Dobson was born on 8 October 1949 inRinteln,Germany, where his father, Arthur Dobson was commissioned as an officer.[1][3] Both Arthur Dobson and Christopher Dobson's mother, Mabel Dobson (née Pollard), were originally fromBradford inYorkshire and had left school at age 14.[3] Dobson had two older siblings, Graham and Gillian.[3] Due to his father's postings, Dobson also lived inLagos,Nigeria.[3]
He is well known for his serendipitous discovery that ordinary proteins can misfold and aggregate to formamyloid structures.[3]
"A postdoc who left his sample of an unfolded protein in an NMR [nuclear magnetic resonance] spectrometer over a long weekend discovered, on his return, that it had turned into a gel. We were curious about this phenomenon and found that the NMR tube was full of amyloid fibrils that we then thought were associated only with diseases".
Dobson authored and co-authored over 800 papers and review articles,[8] including 38 inNature,Science andCell, which have been cited over 100,000 times.[9] As of 2019[update] hisH-index is 153.[9]
In 2012, Dobson founded the Cambridge Centre for Misfolding Diseases,[3] which is currently based in the Chemistry of Health building at the Department of Chemistry at the University of Cambridge.[10][11]
In 2016, Chris Dobson co-founded Wren Therapeutics, a biotechnology start-up company whose mission is to find new therapeutics for Alzheimer's disease.[12][6][13]
Dobson wasknighted in the2018 Queen's Birthday Honours for his contributions to science and higher education.[8][12][14] In 2009, Dobson was awarded theRoyal Medal by the Royal Society "for his outstanding contributions to the understanding of the mechanisms of protein folding and mis-folding, and the implications for disease", and in 2014 he received both the Heineken Prize for Biochemistry and Biophysics and theFeltrinelli International Prize for Medicine. Dobson was elected aFellow of the Royal Society (FRS) in 1996.[15][16] His nomination reads:
Dobson is distinguished for his studies, principally usingNMR methods, of the structures and dynamics of proteins in solution. Such studies include those onlysozyme, with which he demonstrated many methodological advances,interleukin-4, with which he established for the first time the topology of the important family ofhaemopoietic helicalcytokines, andurokinase-typeplasminogen activator, with which he elucidated the dynamic characteristics of multidomainfibrinolytic proteins, Dobson is a pioneer in the application of NMR methods to the problem of protein folding, which is now the major theme of his work. His studies on lysozyme are resulting in one of the most detailed descriptions of a folding pathway for a protein. Dobson has explored the properties and reactions of molecules in solids by means of NMR spectroscopy, includingproteins,organometallic compounds,inorganicparamagnets and the silicaceous components of hydraulic materials. Notable here are analyses of the nature and origin of dynamic properties in molecular solids, and their relationship to structure and reactivity.[17]
Dobson mentored and supervised many notablePhD students andpost-doctoral researchers, many of whom became renowned experts in their own field. These include:
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